SG-Chymotrypsin™

SG-Chymotrypsin™

SG-Chymotrypsin™ is a serine endopeptidase, which predominantly cleaves peptide bonds on the carboxy side of tyrosine, phenylalanine and tryptophan. In addition, chymotrypsin has a low catalytic activity against the carboxy side of leucine, methionine, alanine, aspartic and glutamic acids. It is therefore recommended to always use the shortest digestion time possible.

SG-Chymotrypsin™ is first treated with TLCK to inhibit trypsin that may be present and then subjected to an extensive purification process to remove contaminating protease and chymotryptic autolysis by-products. The highly purified enzyme is then chemically modified to increase its resistance to autolysis and stability.

For protein digestion 5ng/µl SG-Chymotrypsin is typically added to the protein at a ratio of 1:20 to 1:100 enzyme to protein, by weight in a standard digestion buffer. Incubate at 37°C for 2 to 10 hours, but can be extended to 24 hours, due to the extended life of the SG-Chymotrypsin™. We recommend choosing a ratio of enzyme to protein that allows for the shortest incubation time possible. This will reduce or eliminate the catalyzed hydrolysis of peptide bonds with non-aromatic amino acid residues.

Features

Modified Chymotrypsin for sequence analysis.

Resistant to autolysis and degradation.

High Specificity, free from other known endopeptidases.

Consistency of activity levels from lot to lot for reproducible digestions.